GIUSEPPE ZANOTTI

Who I am

I graduated in Chemistry from the University of Padua in 1974, with a thesis on the X-ray structure of bovine pancreatic ribonuclease. From there began a journey that led me to explore the world of molecules, crystals, and proteins.

I worked first as a research fellow, then as a visiting fellow in Oxford, and later as Full Professor of General and Inorganic Chemistry, and subsequently of Biological Chemistry, always at the University of Padua. From 2009 until my retirement in October 2021, I taught at the Department of Biomedical Sciences.

BOOKSBOOKS

MANUALSMANUALS

PUBLICATIONSPUBLICATIONS

Numbers and awards

Some data synthesizing my scientific career, from publications, research and academic awards.

232Papers on international scientific journals

17Book chapters

166Structures deposited at the Protein Data Bank (rcsb.org)

43H-index

6856Citazioni (Scopus)

147I-10 H-index

2007Year of gold medal from AIC (Italian Crystallographic Association)

Research Areas

My research has always focused on a simple and infinite question: what is living matter made of?

Since the very beginning, I studied the structure of molecules and macromolecules using X-ray diffraction. In the 1970s I worked on small molecules, but it was in Oxford, between 1979 and 1980, that I took part in solving the crystal structure of glycogen phosphorylase b.

After returning to Padua, I focused on proteins that bind and transport hydrophobic molecules, such as retinoids and fatty acids. I later worked on protein kinases, in particular CK2, and on its complexes with various inhibitors.

In the 2000s, I began working on bacterial proteins, with a specific focus on those of Helicobacter pylori. My research group solved more than fifteen protein structures involved in the bacterium’s survival and pathogenicity, including those encoded by genes of the cag pathogenicity island from Helicobacter pylori.

My research group solved more than fifteen protein structures involved in the bacterium’s survival and pathogenicity, including those encoded by genes of the cag pathogenicity island.

In recent years, I have adopted cryo-EM, solving near-atomic structures of macromolecular complexes such as the tetanus toxin–antigen complex, photosystem II, the serine protease HtrA, and potato virus X.

Alongside experimental research, I have always cultivated an interest in the theoretical aspects of crystallography. I have published papers on methods for solving the phase problem using Hilbert transforms.

In the field of structural biology, I proposed the concept of tensegrity as a unifying model for understanding the folding of globular proteins.